2ACF

NMR STRUCTURE OF SARS-COV NON-STRUCTURAL PROTEIN NSP3A (SARS1) FROM SARS CORONAVIRUS

2ACF の概要

• エントリーDOI: 10.2210/pdb2acf/pdb
• 分子名称: Replicase polyprotein 1ab, GLYCEROL (3 entities in total)
• 機能のキーワード: adrp domain, sars nsp-3, appr-1-p phosphatase, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, viral protein
• 由来する生物種: SARS coronavirus Tor2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 79871.84

構造登録者

Saikatendu, K.S.,Joseph, J.S.,Subramanian, V.,Neuman, B.W.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Joint Center for Structural Genomics (JCSG) (登録日: 2005-07-18, 公開日: 2006-02-14, 最終更新日: 2024-02-14)

主引用文献

Saikatendu, K.S.,Joseph, J.S.,Subramanian, V.,Clayton, T.,Griffith, M.,Moy, K.,Velasquez, J.,Neuman, B.W.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.
Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.
Structure, 13:1665-1675, 2005

PubMed Abstract: The crystal structure of a conserved domain of nonstructural protein 3 (nsP3) from severe acute respiratory syndrome coronavirus (SARS-CoV) has been solved by single-wavelength anomalous dispersion to 1.4 A resolution. The structure of this "X" domain, seen in many single-stranded RNA viruses, reveals a three-layered alpha/beta/alpha core with a macro-H2A-like fold. The putative active site is a solvent-exposed cleft that is conserved in its three structural homologs, yeast Ymx7, Archeoglobus fulgidus AF1521, and Er58 from E. coli. Its sequence is similar to yeast YBR022W (also known as Poa1P), a known phosphatase that acts on ADP-ribose-1''-phosphate (Appr-1''-p). The SARS nsP3 domain readily removes the 1'' phosphate group from Appr-1''-p in in vitro assays, confirming its phosphatase activity. Sequence and structure comparison of all known macro-H2A domains combined with available functional data suggests that proteins of this superfamily form an emerging group of nucleotide phosphatases that dephosphorylate Appr-1''-p.

PubMed: 16271890
DOI: 10.1016/j.str.2005.07.022

実験手法

X-RAY DIFFRACTION (1.4 Å)